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Oct 01, 2011 · Ordered ATP hydrolysis in the γ complex clamp loader AAA + machine J Biol Chem, 278 ( 2003 ), pp. 14406 - 14413 Article Download PDF View Record in Scopus Google Scholar
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Apr 30, 2008 · Johnson A, O'Donnell M: Ordered ATP hydrolysis in the gamma complex clamp loader AAA+ machine. J Biol Chem. 2003, 278: 14406-14413. 10.1074/jbc.M212708200. PubMed CAS …
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May 02, 2016 · et al.) describe how global ATP hydrolysis and Pi release leads to a strained conformation whereby the SNARE complex is ripped apart in one coordinated event. Such a mechanism may be shared by many other AAA 1 members. The clamp loader is a device which loads the ring-like slid-ing clamp onto double-stranded DNA which in turn induces
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Feb 17, 2012 · The bacteriophage T4 gp44/62 clamp loader also hydrolyzes all bound ATP at the same rate in the presence of gp45 clamp and DNA. 28 Third, convergence between the number of ATP molecules hydrolyzed rapidly by γ complex, which has three ATP-binding sites, 29 and RFC, which has five ATP-binding (four ATPase active) sites, implies that hydrolysis of three ATP molecules in a …
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ing clamps on DNA is performed by the clamp loader assembly in a reaction fueled by ATP (12). In bacteria, the clamp loader is composed of 7 unique subunits (γ, δ, δ, χ, ψ) and the β 2 dimer is the processivity clamp. The clamp loader is an AAA+ ATPase and is the bacterial homologue of the eukaryotic replication factor C (RFC) (7, 8).
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May 02, 2016 · et al.) describe how global ATP hydrolysis and Pi release leads to a strained conformation whereby the SNARE complex is ripped apart in one coordinated event. Such a mechanism may be shared by many other AAA 1 members. The clamp loader is a device which loads the ring-like slid-ing clamp onto double-stranded DNA which in turn induces
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states. For AAA+ machines such as the y complex clamp loader, the chemical energy of ATP hydrolysis activity is transduced into mechanical changes in the clamp loader structure. As a AAA+ machine, y complex clamp loader could be described as a molecular matchmaker. The y complex modifies a protein (i.e., p clamp) such that it
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Nov 15, 2012 · The clamp loader, γ complex, is a member of the AAA + family of ATPase enzymes, which are characterized by the use of ATP binding and hydrolysis to drive reactions that typically relocate or rearrange macromolecules (reviewed in Refs. 14–16).
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bind ATP yet opens the clamp using the energy derived Clamp loaders in various organisms The E. coli clamp loader . Biochemical and structural studies of the γ-complex and its β-clamp have led to a detailed view of how this clamp loader functions. The β-clamp is a ring-shaped oligomer that is composed of two crescent-shaped subunits 2 that
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Nov 15, 2012 · The clamp loader, γ complex, is a member of the AAA + family of ATPase enzymes, which are characterized by the use of ATP binding and hydrolysis to drive reactions that typically relocate or rearrange macromolecules (reviewed in Refs. 14–16).
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Although ATP hydrolysis may contribute to ring opening within T4 (discussed below), detailed studies over the last 20 years or so have revealed that ATP hydrolysis primarily serves to modulate the interaction between clamp loaders and PT DNA by allowing interconversion between high- and low-affinity DNA-binding states.
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Feb 28, 2014 · Clamp loaders belong to a family of proteins known as ATPases associated with various cellular activities (AAA+). These proteins utilize the energy from ATP binding and hydrolysis to perform cellular functions. The clamp loader is required to load the clamp onto DNA for use by DNA polymerases to increase processivity.
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Sep 15, 2009 · An earlier study suggested that the clamp loader associated with the DNA polymerase III holoenzyme could load a clamp on the leading strand without hydrolyzing ATP, but required ATP hydrolysis to load a second clamp on the lagging strand . However, in our FRET assay, two phases of clamp release, one preceding and one following ATP hydrolysis
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Sep 23, 2021 · 43 Primer-template binding to the ternary complex triggers ATP 44 hydrolysis in the clamp loader, followed by sliding clamp closure 45 and ultimately release of the clamp loader complex (Chen et al., 46 2009). Therefore, RFC has two macromolecular substrates, PCNA 47 and p/t-DNA, that must bind sequentially. Yet how clamp loaders
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clamp loading machine. The subunit is referred to as the wrench of the clamp loader, since it can open the dimer at one interface on its own (17–20). The energy for ring opening is not derived from ATP (neither nor bind ATP) but from the energy of protein-protein interaction between and (17). In the absence of ATP, the complex does not bind (18).
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Feb 18, 2020 · In order to visualize how the clamp loader interacts with the sliding clamp, we formed a complex of hRFC with PCNA and the Figure 1. Human clamp loader (hRFC) composition and function. triggers ATP hydrolysis, clamp closure, and clamp loader ejection. available under aCC-BY-NC-ND 4.0 International license.
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Relevant features of the bacterial clamp loader complex and of γ ATPase. (A) The sequence of events mediated by the γ clamp loader [reviewed in (53, 54)].The γ complex consists of five semicircularly arranged subunits (1 δ, 1 δ′ and 3 γ) that in the presence of ATP bind to and open the β clamp.
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